Cations modulate the substrate specificity of bifunctional class I O-methyltransferase from Ammi majus.

@article{Lukain2004CationsMT,
  title={Cations modulate the substrate specificity of bifunctional class I O-methyltransferase from Ammi majus.},
  author={Richard Luka{\vc}in and Ulrich Matern and Silvia Specker and Thomas Joesf Vogt},
  journal={FEBS letters},
  year={2004},
  volume={577 3},
  pages={367-70}
}
Caffeoyl-coenzyme A O-methyltransferase cDNA was cloned from dark-grown Ammi majus L. (Apiaceae) cells treated with a crude fungal elicitor and the open reading frame was expressed in Escherichia coli. The translated polypeptide of 27.1-kDa shared significant identity to other members of this highly conserved class of proteins and was 98.8% identical to the corresponding O-methyltransferase from parsley. For biochemical characterization, the recombinant enzyme could be purified to apparent… CONTINUE READING
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